pubmed.ncbi.nlm.nih.gov

Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself - PubMed

️Invalid Date

Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself

R N Harty et al. J Gen Virol. 1995 Nov.

Abstract

A mammalian two-hybrid system was used to characterize protein-protein interactions between the measles virus nucleoprotein (N) and phosphoprotein (P). Progressive deletions at both the amino- and carboxy-termini of P facilitated the mapping of two distinct domains on P that are important for interaction with N: (i) a domain mapping predominantly within the C-terminal 100 amino acids and (ii) a domain composed of the extreme amino-terminal residues. Using the same two-hybrid assay, we discovered that the P protein interacts strongly with itself. In contrast to the N-P interaction, only a single C-proximal domain of P was essential for P-P interaction.

PubMed Disclaimer

Cited by

The C Protein Is Recruited to Measles Virus Ribonucleocapsids by the Phosphoprotein.
Pfaller CK, Bloyet LM, Donohue RC, Huff AL, Bartemes WP, Yousaf I, Urzua E, Clavière M, Zachary M, de Masson d'Autume V, Carson S, Schieferecke AJ, Meyer AJ, Gerlier D, Cattaneo R. Pfaller CK, et al. J Virol. 2020 Jan 31;94(4):e01733-19. doi: 10.1128/JVI.01733-19. Print 2020 Jan 31. J Virol. 2020. PMID: 31748390 Free PMC article.
An amino acid of human parainfluenza virus type 3 nucleoprotein is critical for template function and cytoplasmic inclusion body formation.
Zhang S, Chen L, Zhang G, Yan Q, Yang X, Ding B, Tang Q, Sun S, Hu Z, Chen M. Zhang S, et al. J Virol. 2013 Nov;87(22):12457-70. doi: 10.1128/JVI.01565-13. Epub 2013 Sep 11. J Virol. 2013. PMID: 24027324 Free PMC article.
Crystal Structure of the Measles Virus Nucleoprotein Core in Complex with an N-Terminal Region of Phosphoprotein.
Guryanov SG, Liljeroos L, Kasaragod P, Kajander T, Butcher SJ. Guryanov SG, et al. J Virol. 2015 Dec 30;90(6):2849-57. doi: 10.1128/JVI.02865-15. J Virol. 2015. PMID: 26719278 Free PMC article.
Homo-oligomerization of Marburgvirus VP35 is essential for its function in replication and transcription.
Möller P, Pariente N, Klenk HD, Becker S. Möller P, et al. J Virol. 2005 Dec;79(23):14876-86. doi: 10.1128/JVI.79.23.14876-14886.2005. J Virol. 2005. PMID: 16282487 Free PMC article.
Comparison of predicted amino acid sequences of measles virus strains in the Edmonston vaccine lineage.
Parks CL, Lerch RA, Walpita P, Wang HP, Sidhu MS, Udem SA. Parks CL, et al. J Virol. 2001 Jan;75(2):910-20. doi: 10.1128/JVI.75.2.910-920.2001. J Virol. 2001. PMID: 11134304 Free PMC article.

Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself - PubMed